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1 t two of the five cysteine residues in human glutaredoxin.
2 nzymes such as glutathione S-transferase and glutaredoxin.
3 from immobilized S-glutathionylated actin to glutaredoxin.
4 the reactivation of RNR through reduction of glutaredoxins.
5 isulfide on par with mammalian and bacterial glutaredoxins.
6 es required for synthesis of glutathione and glutaredoxins.
7 cystine reductase activity characteristic of glutaredoxins.
8 member of this new expanding family of large glutaredoxins.
9 lications for protein disulfide reduction by glutaredoxins.
10 reducing proteins glutaredoxin 3 (Grx3) and glutaredoxin 1 (Grx1) are structurally similar but exhib
11 hione redox couple: Inhibition of endogenous glutaredoxin 1 (Grx1) disrupted roGFP2 responses to O(3)
18 Strains that lack thioredoxins 1 and 2 and glutaredoxin 1 do not grow because RNR remains in its ox
19 storing the ability of Atox1 to bind copper; glutaredoxin 1 facilitates this reaction when GSH is low
20 eak Na(+)-K(+) pump current when we included glutaredoxin 1 in patch pipette solutions to reverse glu
21 lically stressed monocytes by overexpressing glutaredoxin 1 protected MKP-1 from degradation and norm
23 G, proline increased the expression of grxA (glutaredoxin 1) and trxC (thioredoxin 2) of the OxyR reg
24 edoxin superfamily, thioredoxins 1 and 2 and glutaredoxin 1, is unable to grow, a phenotype presumed
31 in lungs of mice lacking and overexpressing glutaredoxin-1 (Glrx1), and wild-type (WT) mice in respo
35 catalase, a dominant-negative p47(phox), or glutaredoxin-1 decreased GSS-Ras, Ras activation, p38, a
36 promotes clearance of P. aeruginosa and that glutaredoxin-1 impairs bacterial clearance and increases
38 n of SERCA, and adenoviral overexpression of glutaredoxin-1 prevented both the HNO-stimulated oxidati
39 PTMs of SirT1 are glutathione (GSH) adducts, glutaredoxin-1 was overexpressed to remove this modifica
40 ss spectroscopy, five proteins, cathepsin G, glutaredoxin-1, thioredoxin, GP1b, and fibrinogen, showe
46 revealed that morpholino-based knockdown of glutaredoxin 2 in zebrafish, a model organism to study v
49 ryogenesis has recently been exemplified for glutaredoxin 2, a vertebrate-specific glutathione-disulf
50 ion of a functional vascular system requires glutaredoxin 2-dependent reversible S-glutathionylation
59 ations that lead to RNR overproduction allow glutaredoxin 3 to reduce sufficient RNR for growth of th
60 cell allows more effective interaction with glutaredoxin 3, thus restoring an effective pool of deox
62 tional role of the interaction between human glutaredoxin-3 (GRX3) and its protein partner BOLA2, we
63 [2Fe-2S]-bridged heterodimer formed between glutaredoxin-3 and the BolA-like protein Fe repressor of
65 racterization tool is demonstrated with holo glutaredoxin 5 (GLRX5) homodimer and holo GLRX5:BolA-lik
68 that Ssq1 also interacts with the monothiol glutaredoxin 5 (Grx5) at a binding site different from t
71 zebrafish mutants is caused by deficiency of glutaredoxin 5 (grx5), a gene required in yeast for Fe-S
72 de a sideroblastic anemia with deficiency of glutaredoxin 5 and a myopathy associated with a deficien
73 ever, the human diseases, Friedreich ataxia, glutaredoxin 5-deficient sideroblastic anemia, ISCU myop
75 eved with the reduced form of glutathione or glutaredoxin, a protein known to replace thioredoxin in
79 ng (13)C-labeled glucose, and an increase in glutaredoxin activity, which catalyzes the glutathione-d
80 sults reveal a novel neuroprotective role of glutaredoxin against dopaminergic neurodegeneration in m
82 ndings thus indicate that carefully balanced glutaredoxin amounts in the IMS ensure efficient oxidati
83 balance between cellular reductants such as glutaredoxin and copper activation pathways in controlli
84 ese results present a physiological role for glutaredoxin and ROS- induced reversible actin glutathio
85 ow that H encodes a novel epidermis-specific glutaredoxin and that the pattern of trichome distributi
87 Using these proteins, we showed that the glutaredoxin and thioredoxin reductase domains of TGR co
93 h a high amino acid sequence similarity with glutaredoxins and mycoredoxins but with a thioredoxin-li
96 ative participation of the thioltransferase (glutaredoxin) and thioredoxin systems in overall cellula
98 including glucanase, glutathione peroxidase, glutaredoxin, and a profilin were found to be widely exp
99 lular thiol oxidoreductases, thioredoxin and glutaredoxin, and found that these enzymes can control t
100 Glutathione S-transferase, thioredoxin, glutaredoxins, and DNA repair enzymes responded most str
101 d enzymes, including glutathione reductases, glutaredoxins, and glutathione S-transferases, indicated
102 we conclude that catalase and peroxiredoxin-glutaredoxin are determinants of bacterial persistence d
103 E10R and L1R viral membrane proteins and the glutaredoxin are in the cytoplasm, in which assembly of
104 stically in fungi and higher eukaryotes, the glutaredoxins are conserved, yet their precise function
110 we demonstrate that an Arabidopsis monothiol glutaredoxin, AtGRXS17 (At4g04950), plays a critical rol
111 ich has a redox potential similar to that of glutaredoxin, becomes essential for cell survival when G
112 se, superoxide dismutases, thioredoxins, and glutaredoxins between normal Prdx6-/- and Prdx6+/+ mice
113 po-form of A4V SOD1 was highly reactive with glutaredoxin but not SOD1 containing both copper and zin
114 isulfides, containing one adducted toxin per glutaredoxin but with elimination of two sulfur atoms fr
115 Escherichia coli is distinguished from other glutaredoxins by its larger size, low overall sequence i
117 subclass of the thioredoxin superfamily, the glutaredoxins, can become disulfide bond-formation catal
118 g to Grx1(as) cDNA showed that two different glutaredoxin cDNAs (Grx1(as) and Grx1) were generated fr
119 es within the DsbA family different from the glutaredoxin cluster to which mycoredoxin-1 (Mrx1 or Rv3
122 e observed that the catalytic enhancement by glutaredoxin could be ascribed fully to the difference b
124 concentration of inducer, and the amount of glutaredoxin could be varied from barely detectable to g
125 Physiological reductases, thioredoxins and glutaredoxins, could not dissolve AtGAPC1 aggregates but
126 ave identified mutations in the gene Grxcr1 (glutaredoxin cysteine-rich 1) in five independent alleli
127 nt in GSH biosynthesis) that is defective in glutaredoxin-dependent redox signaling and ntra/ntrb (de
128 ly complex proteins or deletion of cytosolic glutaredoxins did not reduce expression of Yap5 target g
130 edoxin reductases, it contains an N-terminal glutaredoxin domain and exhibits a wide spectrum of enzy
135 ged between a BOLA2 molecule and a monothiol glutaredoxin domain of GRX3, and to transfer both [2Fe-2
137 to 72 forming a classical "thioredoxin-fold" glutaredoxin domain, connected by an 11 residue linker t
142 ed by hktE) and a bifunctional peroxiredoxin-glutaredoxin (encoded by pdgX) in resistance of NTHI to
143 catalase-peroxidase system, but thioredoxin/glutaredoxin enzymes might alleviate oxidative stress.
144 Importantly, treatment of inactive KGDH with glutaredoxin facilitated the GSH-dependent recovery of K
145 interaction between members of the monothiol glutaredoxin family and members of the BolA-like protein
146 ld type highlights the role of mitochondrial glutaredoxin Fe-S-binding in whole plant growth and toxi
148 signaling and that cytokinins could activate glutaredoxin gene expression independent of plant nitrat
149 We determined that nitrate induction of glutaredoxin gene expression was dependent upon cytokini
150 h2 mutation was caused by transposition of a glutaredoxin gene, MALE STERILE CONVERTED ANTHER1 (MSCA1
154 se clusters are transferred to the monothiol glutaredoxin GLRX5 by an Hsp70 system followed by insert
155 substrates are protein disulfide isomerase, glutaredoxin, glutathione peroxidase, NK-lysin/granulysi
156 Thus, thioredoxin was more efficient than glutaredoxin, glutathione, or a 14-kDa thioredoxin-like
158 as composed of a basic TR1 module fused to a glutaredoxin (Grx) domain that contained an unusual acti
161 nhibitory RNA (siRNA) directed against GR or glutaredoxin (Grx) potentiated adriamycin-induced macrop
162 mulator fern Pteris vittata L., a cDNA for a glutaredoxin (Grx) Pv5-6 was isolated from a frond expre
168 oxidoreductase component of the GSH system, glutaredoxin (Grx), is involved in the reduction of GSH-
169 onylation of IKK-beta Cys-179 is reversed by glutaredoxin (GRX), which restores kinase activity.
174 is catalyzed specifically and efficiently by glutaredoxin (GRx, thioltransferase), a thioldisulfide o
175 ard mixed disulfides between glutathione and glutaredoxin (Grx-S-SG), consistent with the in vivo req
177 edox) changes in the glutathione pool (GSH), glutaredoxins (GRX) and thioredoxins (TRX) are important
178 ns of oxidative stress and are controlled by glutaredoxins (Grx) that, under physiological conditions
179 (1) Several recent reports have demonstrated glutaredoxins (Grx) to form [Fe(2)S(2)] cluster-bridged
180 [2Fe-2S]-containing complexes with monothiol glutaredoxins (Grx), structural details are lacking.
182 il cDNA library, using a (32)P-labeled human glutaredoxin (Grx1) cDNA probe under non-stringent condi
183 frame of the previously reported first human glutaredoxin (Grx1) cDNA, but the 3'-untranslated region
185 contains two gene pairs encoding cytoplasmic glutaredoxins (GRX1, GRX2) and thioredoxins (TRX1, TRX2)
186 the form of [2Fe-2S]-GSH2 from the monothiol glutaredoxin Grx3/4, and the same electron source, in th
187 We presently show that the nuclear monothiol glutaredoxins Grx3 and Grx4 are critical for iron inhibi
188 A homologue Fra2 and the cytosolic monothiol glutaredoxins Grx3 and Grx4 together play a key role in
189 likely dependent on the cytosolic monothiol glutaredoxins Grx3/Grx4 and the Fe-S cluster protein Dre
190 athway that includes the cytosolic monothiol glutaredoxins (Grx3 and Grx4) and the BolA homologue Fra
191 NG1 to suppress disease susceptibility genes glutaredoxins GRX480, GRXS13 and thioredoxin TRX-h5.
194 arlier in Fe-S biogenesis with the monothiol glutaredoxin, Grx5, and Bol3 functions late with Nfu1.
195 roteins, accessory factors such as monothiol glutaredoxin, GrxD, and the FeS carrier protein NfuA are
196 structural similarity, CxxC/S-type (class I) glutaredoxins (Grxs) act as oxidoreductases, while CGFS-
206 ete reactivation was only possible using the glutaredoxin/GSH system (97 +/- 4% and 91 +/- 3% for hBC
208 ioned in two activities that are typical for glutaredoxins, hydroxyethyl disulfide reduction and elec
209 ed Srx as the reaction intermediate, whereas glutaredoxin I was more favorable for deglutathionylatin
211 current study sporidesmin inactivated human glutaredoxin in a time- and concentration-dependent mann
212 scU to apo-Grx5, a general purpose monothiol glutaredoxin in A. vinelandii, was monitored by circular
213 recedented role for the thiol oxidoreductase glutaredoxin in reducing the SOD1 disulfide and destabil
214 These data suggest that redox regulation by glutaredoxin in retinal glial cells is perturbed by hype
215 rved role of cytosolic monothiol multidomain glutaredoxins in cellular iron metabolism pathways, incl
219 epidithiopiperazine-2,5-diones to inactivate glutaredoxin indicated that at least one phenyl substitu
220 ubstitutions in the active site of the three glutaredoxins indicated that only the N-terminal cystein
221 specific dethiolase enzyme thioltransferase (glutaredoxin), indicating that the inactivated form of t
222 tranferase), because Cd(II), an inhibitor of glutaredoxin, inhibits intracellular actin deglutathiony
223 s of the oxidized probe with glutathione and glutaredoxin into a larger kinetic model of peroxide met
225 disulfide interchange; either thioredoxin or glutaredoxin is then thought to reduce the cystine that
226 The primary function of Grx2 as a GST-like glutaredoxin is to catalyze reversible glutathionylation
228 n S-glutathionylation, and thioltransferase (glutaredoxin) is a specific and efficient catalyst of pr
234 bolism encode a second thioredoxin (TrxC), a glutaredoxin-like protein and enzymes involved in the bi
237 a and beta subunits of RNR; NrdH and TrxR, a glutaredoxin-like thioredoxin and a thioredoxin reductas
245 ionylation of the alpha subunit catalyzed by glutaredoxin or dithiothreitol resulted in restoration o
247 as reductant directly in the active site, or glutaredoxins or thioredoxins reduce a C-terminal cystei
248 t of the system revealed no interaction with glutaredoxins or thioredoxins, indicating that this clas
250 ion are delivered by a redoxin (thioredoxin, glutaredoxin, or NrdH) via a pair of conserved active si
251 the single-cysteine omega class, which have glutaredoxin oxidoreductase activity rather than GSH-S-t
256 These include catalase (HktE), peroxiredoxin/glutaredoxin (PgdX), and a ferritin-like protein (Dps).
258 olds have diverged from a common thioredoxin/glutaredoxin progenitor but did so by different mechanis
259 tein that contains a region of similarity to glutaredoxin proteins and a cysteine-rich region at its
260 IMS and show that limiting amounts of these glutaredoxins provide a kinetic barrier to prevent the t
262 owing that a poplar ortholog is reduced by a glutaredoxin rather than NADP-thioredoxin reductase.
263 d (glutathione S-transferase P) and reverse (glutaredoxin) reactions creates a functional cycle that
264 n Bacteroides fragilis lacks the glutathione/glutaredoxin redox system and possesses an extensive num
268 ally characterized the role of mitochondrial glutaredoxin S15 (GRXS15) in biogenesis of ISC containin
270 " cytokinin-deficient plants and "long-root" glutaredoxin-silenced plants generated hybrids that disp
271 se has been shown to require glutathione and glutaredoxin, suggesting that thiol chemistry might be i
274 e redox Western blot data indicated that the glutaredoxin system protected Trx1 in HeLa cells from ox
275 lutathionylation of hBCATc-SSG using the GSH/glutaredoxin system provides evidence that this protein
276 ts strongly suggest that the thioredoxin and glutaredoxin systems are the key regulators for hSOD1 ag
278 reased the capability of the thioredoxin and glutaredoxin systems to reduce hSOD1 compared with wild-
279 The carboxyl-terminal domain functions as a glutaredoxin that mediates the transfer of electrons fro
280 of intramolecular disulfide bonds of the G4L glutaredoxin, the L1R membrane protein, and the structur
282 lutathionylation is most likely catalyzed by glutaredoxin (thioltranferase), because Cd(II), an inhib
284 osphatases using a descriptor built from the glutaredoxin/thioredoxin family, proteins that have no a
285 iosynthetic enzymes, glutathione reductases, glutaredoxins, thioredoxins, and thioredoxin reductases,
286 d disulfide with GSH before being reduced by glutaredoxin to regenerate the active Acr2p reductase.
287 d disulfide with GSH before being reduced by glutaredoxin to regenerate the active ArsC reductase.
289 of [2Fe-2S] cluster transfer from monothiol glutaredoxins to target proteins is a fundamental, but s
290 Aspartic proteases, BTB/POZ proteins (BTB), Glutaredoxins, Trypsin alpha-amylase inhibitor proteins,
291 n-associated protein, focal adhesion kinase, glutaredoxin, utrophin) may be novel mediators of NFT fo
296 iamide-GSH is partially recovered by DTT and glutaredoxin, whereas the disulfide linkage of GSH with
297 ytosolic compartment that involves monothiol glutaredoxins, which bind iron in the form of iron-sulfu
298 al member of a ubiquitous class of monothiol glutaredoxins with a strictly conserved CGFS active-site
299 th the help of thioredoxin reductase and the glutaredoxins with the small molecule glutathione and gl
300 pathways via either the thioredoxins or the glutaredoxins without, evidently, the intermediary of gl